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O42227

- HDA1B_XENLA

UniProt

O42227 - HDA1B_XENLA

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Protein

Probable histone deacetylase 1-B

Gene

hdac1-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.1 Publication

Catalytic activityi

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei141 – 1411By similarity

GO - Molecular functioni

  1. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  2. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
  3. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
  4. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Probable histone deacetylase 1-B (EC:3.5.1.98)
Short name:
HD1-B
Alternative name(s):
RPD3 homolog
Gene namesi
Name:hdac1-b
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-865283. hdac1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi141 – 1411H → A: Abolishes histone deacetylase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 480480Probable histone deacetylase 1-BPRO_0000114692Add
BLAST

Proteomic databases

PRIDEiO42227.

Interactioni

Subunit structurei

Found in a large complex with RBBP4 and MI-2.1 Publication

Structurei

3D structure databases

ProteinModelPortaliO42227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 321312Histone deacetylaseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi299 – 3024Poly-Gly

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG057112.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSiPR01270. HDASUPER.
PR01271. HISDACETLASE.

Sequencei

Sequence statusi: Complete.

O42227-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALSQGTKKK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK
60 70 80 90 100
MEIYRPHKAS AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC
110 120 130 140 150
PVFDGLFEFC QLSTGGSVAS AVKLNKQQTD ISVNWSGGLH HAKKSEASGF
160 170 180 190 200
CYVNDIVLAI LELLKYHQRV VYIDIDIHHG DGVEEAFYTT DRVMSVSFHK
210 220 230 240 250
YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI FKPVMTKVME
260 270 280 290 300
MFQPSAVVLQ CGADSLSGDR LGCFNLTIKG HAKCVEFIKT FNLPMLMLGG
310 320 330 340 350
GGYTIRNVAR CWTYETAVAL DSEIPNELPY NDYFEYFGPD FKLHISPSNM
360 370 380 390 400
TNQNTNEYLE KIKQRLFENL RMLPHAPGVQ MQAIPEDSVH DDSGEEDEED
410 420 430 440 450
PDKRISIRSS DKRIACDEEF SDSEDEGEGG RKNVANFKKV KRVKTEEEKE
460 470 480
GEDKKDVKEE EKAKDEKTDS KRVKEETKSV
Length:480
Mass (Da):54,893
Last modified:January 1, 1998 - v1
Checksum:iCA92DE34D36E39E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020658 mRNA. Translation: AAC60346.1.
UniGeneiXl.20805.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020658 mRNA. Translation: AAC60346.1 .
UniGenei Xl.20805.

3D structure databases

ProteinModelPortali O42227.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi O42227.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Xenbasei XB-GENE-865283. hdac1.

Phylogenomic databases

HOVERGENi HBG057112.

Family and domain databases

Gene3Di 3.40.800.20. 1 hit.
InterProi IPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view ]
PANTHERi PTHR10625. PTHR10625. 1 hit.
Pfami PF00850. Hist_deacetyl. 1 hit.
[Graphical view ]
PIRSFi PIRSF037913. His_deacetylse_1. 1 hit.
PRINTSi PR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNeti Search...

Publicationsi

  1. "Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase."
    Wong J., Patterton D., Imhof A., Guschin D., Shi Y.-B., Wolffe A.P.
    EMBO J. 17:520-534(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase."
    Wade P.A., Jones P.L., Vermaak D., Wolffe A.P.
    Curr. Biol. 8:843-846(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH RBBP4 AND MI-2.
  3. "Functional analysis of the SIN3-histone deacetylase RPD3-RbAp48-histone H4 connection in the Xenopus oocyte."
    Vermaak D., Wade P.A., Jones P.L., Shi Y.-B., Wolffe A.P.
    Mol. Cell. Biol. 19:5847-5860(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RBBP4, MUTAGENESIS OF HIS-141.

Entry informationi

Entry nameiHDA1B_XENLA
AccessioniPrimary (citable) accession number: O42227
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3